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== | ==Crystal structure of the TolB(P201C)-ColicinE9 TBE peptide(A33C) complex.== | ||
[[http:// | <StructureSection load='4jml' size='340' side='right'caption='[[4jml]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4jml]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Escherichia_coli_DH1 Escherichia coli DH1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JML OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JML FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4jml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jml OCA], [https://pdbe.org/4jml PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jml RCSB], [https://www.ebi.ac.uk/pdbsum/4jml PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jml ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CEA9_ECOLX CEA9_ECOLX] This plasmid-coded bactericidal protein is an endonuclease active on both single- and double-stranded DNA but with undefined specificity. Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Porins are beta-barrel outer-membrane proteins through which small solutes and metabolites diffuse that are also exploited during cell death. We have studied how the bacteriocin colicin E9 (ColE9) assembles a cytotoxic translocon at the surface of Escherichia coli that incorporates the trimeric porin OmpF. Formation of the translocon involved ColE9's unstructured N-terminal domain threading in opposite directions through two OmpF subunits, capturing its target TolB on the other side of the membrane in a fixed orientation that triggers colicin import. Thus, an intrinsically disordered protein can tunnel through the narrow pores of an oligomeric porin to deliver an epitope signal to the cell to initiate cell death. | |||
Intrinsically disordered protein threads through the bacterial outer-membrane porin OmpF.,Housden NG, Hopper JT, Lukoyanova N, Rodriguez-Larrea D, Wojdyla JA, Klein A, Kaminska R, Bayley H, Saibil HR, Robinson CV, Kleanthous C Science. 2013 Jun 28;340(6140):1570-4. doi: 10.1126/science.1237864. PMID:23812713<ref>PMID:23812713</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
< | </div> | ||
[[ | <div class="pdbe-citations 4jml" style="background-color:#fffaf0;"></div> | ||
[[ | |||
==See Also== | |||
[[Category: | *[[Colicin 3D structures|Colicin 3D structures]] | ||
[[Category: | *[[TolB|TolB]] | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Escherichia coli]] | |||
[[Category: Escherichia coli DH1]] | |||
[[Category: Large Structures]] | |||
[[Category: Kleanthous C]] | |||
[[Category: Klein A]] | |||
[[Category: Wojdyla JA]] | |||
Latest revision as of 18:45, 20 September 2023
Crystal structure of the TolB(P201C)-ColicinE9 TBE peptide(A33C) complex.Crystal structure of the TolB(P201C)-ColicinE9 TBE peptide(A33C) complex.
Structural highlights
FunctionCEA9_ECOLX This plasmid-coded bactericidal protein is an endonuclease active on both single- and double-stranded DNA but with undefined specificity. Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria. Publication Abstract from PubMedPorins are beta-barrel outer-membrane proteins through which small solutes and metabolites diffuse that are also exploited during cell death. We have studied how the bacteriocin colicin E9 (ColE9) assembles a cytotoxic translocon at the surface of Escherichia coli that incorporates the trimeric porin OmpF. Formation of the translocon involved ColE9's unstructured N-terminal domain threading in opposite directions through two OmpF subunits, capturing its target TolB on the other side of the membrane in a fixed orientation that triggers colicin import. Thus, an intrinsically disordered protein can tunnel through the narrow pores of an oligomeric porin to deliver an epitope signal to the cell to initiate cell death. Intrinsically disordered protein threads through the bacterial outer-membrane porin OmpF.,Housden NG, Hopper JT, Lukoyanova N, Rodriguez-Larrea D, Wojdyla JA, Klein A, Kaminska R, Bayley H, Saibil HR, Robinson CV, Kleanthous C Science. 2013 Jun 28;340(6140):1570-4. doi: 10.1126/science.1237864. PMID:23812713[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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